Nothing Special   »   [go: up one dir, main page]

Chibber et al., 1974 - Google Patents

[48] Plasminogen

Chibber et al., 1974

Document ID
2931259363807276952
Author
Chibber B
Deutsch D
Mertz E
Publication year
Publication venue
Methods in enzymology

External Links

Snippet

Publisher Summary Plasminogen is the zymogen of the proteolytic enzyme plasmin (EC 3.4. 4.14), the enzyme responsible for the dissolution of fibrin clots in blood. In a continuing effort to resolve problems of homogeneity, yield, stability, reproducibility, solubility at physiological …
Continue reading at www.sciencedirect.com (other versions)

Classifications

    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/48Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6424Serine endopeptidases (3.4.21)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12YENZYMES
    • C12Y304/00Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
    • C12Y304/21Serine endopeptidases (3.4.21)
    • C12Y304/21069Protein C activated (3.4.21.69)
    • YGENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y10TECHNICAL SUBJECTS COVERED BY FORMER USPC
    • Y10STECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y10S435/00Chemistry: molecular biology and microbiology
    • Y10S435/814Enzyme separation or purification
    • Y10S435/815Enzyme separation or purification by sorption

Similar Documents

Publication Publication Date Title
Chibber et al. [48] Plasminogen
Wiman et al. Structural Relationship between “Glutamic Acid” and “Lysine” Forms of Human Plasminogen and Their Interaction with the NH2‐Terminal Activation Peptide as Studied by Affinity Chromatography
Wiman et al. Purification and characterization of human antiplasmin, the fast‐acting plasmin inhibitor in plasma
Lijnen et al. Isolation and characterization of a human plasma protein with affinity for the lysine binding sites in plasminogen. Role in the regulation of fibrinolysis and identification as histidine-rich glycoprotein.
Wallén et al. Purification and identification of two structural variants of porcine tissue plasminogen activator by affinity adsorption on fibrin
Wiman et al. The specific interaction between plasminogen and fibrin. A physiological role of the lysine binding site in plasminogen
Nolan et al. [17] Ancrod, the coagulating enzyme from Malayan pit viper (Agkistrodon rhodostoma) venom
WINN et al. Studies on the lysine‐binding sites of human plasminogen: the effect of ligand structure on the binding of lysine analogs to plasminogen
Violand et al. The effect of ϵ-amino caproic acid on the gross conformation of plasminogen and plasmin
US6670455B1 (en) Process for the preparation in pure form of the protease activating blood clotting VII, its proenzyme or a mixture of both proteins by means of affinity chromatography
Schmer The purification of bovine thrombin by affinity chromatography on benzamidine-agarose
Powell et al. Activation of human neo-plasminogen-Val442 by urokinase and streptokinase and a kinetic characterization of neoplasmin-Val442.
US4137127A (en) Process for the preparation of thrombin-like enzymes from snake venoms
US4898825A (en) Methods for purification of single-chain and double-chain tissue plasminogen activator
EP0124613B1 (en) Novel plasminogen activator derived from human kidneys, process for its preparation, and thrombolytic drug containing the same
ANDO et al. High-performance liquid chromatographic assay of transglutaminase and its application to the purification of human erythrocyte transglutaminase and platelet factor XIII
US4229540A (en) Hydrolase purified from human plasma
JPH0734743B2 (en) Plasminogen activator
EP0276328B1 (en) Process for separating single-strand human tpa and double-strand human tpa from each other
US4957864A (en) Novel plasminogen activator and its preparation process
Nagasawa et al. A simple method for purification of bovine plasminogen
Weinstein et al. Purification and preliminary characterization of rabbit vitamin K-dependent coagulation proteins
Semeraro et al. The Inhibition of Plasmin by Antithrombin–Heparin Complex: I. IN HUMAN PLASMA IN VITRO
US5158882A (en) Method for purifying a crude tissue plasminogen activator preparation
Andersson Purification and studies of components of the haemostatic system by affinity chromatography